ID A0A0X3VBU9_9ACTN Unreviewed; 717 AA.
AC A0A0X3VBU9;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=carbonic anhydrase {ECO:0000256|ARBA:ARBA00012925};
DE EC=4.2.1.1 {ECO:0000256|ARBA:ARBA00012925};
GN ORFNames=ADL15_01685 {ECO:0000313|EMBL:KUL42271.1};
OS Actinoplanes awajinensis subsp. mycoplanecinus.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=135947 {ECO:0000313|EMBL:KUL42271.1, ECO:0000313|Proteomes:UP000053244};
RN [1] {ECO:0000313|EMBL:KUL42271.1, ECO:0000313|Proteomes:UP000053244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16712 {ECO:0000313|EMBL:KUL42271.1,
RC ECO:0000313|Proteomes:UP000053244};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible hydration of carbon dioxide to form
CC bicarbonate. {ECO:0000256|ARBA:ARBA00024993}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17544; EC=4.2.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000943};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC {ECO:0000256|ARBA:ARBA00006217}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUL42271.1}.
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DR EMBL; LLZH01000002; KUL42271.1; -; Genomic_DNA.
DR RefSeq; WP_067684416.1; NZ_LLZH01000002.1.
DR AlphaFoldDB; A0A0X3VBU9; -.
DR OrthoDB; 9771198at2; -.
DR Proteomes; UP000053244; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0015976; P:carbon utilization; IEA:InterPro.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR Gene3D; 3.40.1050.10; Carbonic anhydrase; 1.
DR InterPro; IPR001765; Carbonic_anhydrase.
DR InterPro; IPR015892; Carbonic_anhydrase_CS.
DR InterPro; IPR036874; Carbonic_anhydrase_sf.
DR InterPro; IPR011547; SLC26A/SulP_dom.
DR InterPro; IPR001902; SLC26A/SulP_fam.
DR PANTHER; PTHR11814:SF227; CARBONIC ANHYDRASE; 1.
DR PANTHER; PTHR11814; SULFATE TRANSPORTER; 1.
DR Pfam; PF00484; Pro_CA; 1.
DR Pfam; PF00916; Sulfate_transp; 1.
DR SMART; SM00947; Pro_CA; 1.
DR SUPFAM; SSF53056; beta-carbonic anhydrase, cab; 1.
DR PROSITE; PS00704; PROK_CO2_ANHYDRASE_1; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000053244};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 37..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 79..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 113..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 182..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 231..253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 307..325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 331..350
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 362..391
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 8..358
FT /note="SLC26A/SulP transporter"
FT /evidence="ECO:0000259|Pfam:PF00916"
SQ SEQUENCE 717 AA; 74661 MW; F422F86F14A00CA2 CRC64;
MSDLTQFLRR DLPASIVVFL IAIPLSLGIA AASGAPLLAG LVAAVVGGIV AGALGGAPLQ
VSGPAAGLTV IVAGAVADFG FAGTAAVVAL AGIVQILLGV SRLGRAALAL SPAVVHGMLA
GIGLVIALSQ VHVLLGGAPQ SSAWANLRDL PAQIVEHHSL SAALGLLTIA VLILWPRFVK
VSLLPAALVA VVGVTVLAHV TGADVTRVKL PEEPLAELIT PVWPDAPLRQ ITVAVLTIAL
VASVESLLSA VAVDRMHDGP RARLNKELIG QGAANTVSGL LGGLPVTGVI VRSSTNVAAG
ARTRASAIMH GVWVAAFVLL CAGLLERIPM AVLAAVLIVV GLRLIDLGQI RTYARHRELP
TYLVTAIGVV AVDLLTGVAL GMVTAAAMIL WRLTRCEIQT VEQAPGQWSV NIAGTCAFIE
SARLTREFGA IPPGQEVEVE LHLDYLDHGA FETIKNWAET YEKGGGTVRI REVHDSWFHQ
ATSGRLGSNK STPRLIGSWS RWQGLNHQRR DAMAAGIAEF ERSVAPMVRP HLATLAREGQ
SPEQLFITCA DSRVVPNLIT ASGPGDLFCV RNVGNLVPPH RPAPDHRSRP AAGDTSVGAA
IEYAVDVLGV TTITVCGHSG CGAVRALMSG AAPPGSALGD WLGLSGVHFT DVDDEQRCCT
DNVLQQLANL RTYPVVQAAE AAGRLRITGM YFDIAEALMH QVDPVLGTHR PLHTPAA
//
